Evidence map›Paper›PMID 26840730›Full record

ArticleBiophysical journal2016

Compliance Accelerates Relaxation in Muscle by Allowing Myosin Heads to Move Relative to Actin.

Kenneth S Campbell

Abstract read
In one paragraph

Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed.

  1. Article
  2. Dual-filament regulation of relaxation in mammalian fast skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Hypertrophic cardiomyopathy β-cardiac myosin mutation (P710R) leads to hypercontractility by disrupting super relaxed state.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  5. Article
  6. KBTBD13 is an actin-binding protein that modulates muscle kinetics.The Journal of clinical investigation · 2020
    Article
  7. KBTBD13 and the ever-expanding sarcomeric universe.The Journal of clinical investigation · 2020
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Myocardial relaxation is accelerated by fast stretch, not reduced afterload.Journal of molecular and cellular cardiology · 2017
    Article
  16. Article
  17. Article
  18. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author.

Kenneth S CampbellDivision of Cardiovascular Medicine, Department of Physiology, University of Kentucky, Lexington, Kentucky. Electronic address: k.s.campbell@uky.edu.

Funding

Kentucky Center for Clinical and Translational ScienceUL1TR001998 · NCATS · UNIVERSITY OF KENTUCKY · PI HARTMANN, KATHERINE E, KERN, PHILIP A · 2016 to 2025
$34.2M
Kentucky Center for Clinical and Translational ScienceUL1TR000117 · NCATS · UNIVERSITY OF KENTUCKY · PI KERN, PHILIP A · 2012 to 2015
$13.3M
Dual filament control of myocardial power and hemodynamicsR01HL148785 · NHLBI · UNIVERSITY OF MISSOURI-COLUMBIA · PI Kenneth S Campbell, Thomas Kampourakis · 2020 to 2026
$3.2M
Myocardial Stiffness in Diastolic Heart FailureR01HL090749 · NHLBI · UNIVERSITY OF KENTUCKY · PI CAMPBELL, KENNETH S · 2008 to 2012
$1.6M
NCATS NIH HHS TR000117NCATS NIH HHS UL1 TR000117NCATS NIH HHS UL1 TR001998NHLBI NIH HHS HL090749NHLBI NIH HHS R01 HL090749NHLBI NIH HHS R01 HL148785
6 · The paper itself

Abstract

The mechanisms that limit the speed at which striated muscles relax are poorly understood. This work presents, to our knowledge, novel simulations that show that the time course of relaxation is accelerated by interfilamentary movement resulting from series compliance; force drops faster when myosin heads move relative to actin during relaxation. This insight was obtained by using cross-bridge distribution techniques to simulate the mechanical behavior of half-sarcomeres that were connected in series with springs of varying stiffness. (The springs mimic the combined effects of half-sarcomere heterogeneity and muscle's series elastic component.) Half-sarcomeres that shortened by >∼10 nm when they were activated subsequently relaxed with a biphasic profile; force initially declined slowly and approximately linearly before collapsing with a fast exponential time course. Stretches imposed during the linear phase quickened relaxation, while shortening movements prolonged the time course. These predictions are consistent with data from experiments performed by many other groups using single muscle fibers and isolated myofibrils. When half-sarcomeres were linked to stiff springs (so that they did not shorten appreciably during the simulations), force relaxed with a slow exponential time course and did not show biphasic behavior. Together, these results suggest that fast relaxation of striated muscle is an emergent property that reflects multiscale interactions within the muscle architecture. The nonlinear behavior during relaxation reflects perturbations to the dynamic coupling of regulated binding sites and cycling myosin heads that are induced by interfilamentary movement.

Indexed as

Muscle RelaxationAccelerationActinsAnimalsElasticityHumansModels, TheoreticalSarcomeresSkeletal Muscle MyosinsActinsSkeletal Muscle Myosins

Identifiers

PMID26840730
PMCPMC4744171

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.